MMAB

For other uses, see MMAB (disambiguation).

MMAB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2IDX
Identifiers
Aliases	MMAB , ATR, CFAP23, cblB, cob, methylmalonic aciduria (cobalamin deficiency) cblB type, metabolism of cobalamin associated B
External IDs	OMIM: 607568; MGI: 1924947; HomoloGene: 12680; GeneCards: MMAB; OMA:MMAB - orthologs
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12q24.11 Start 109,553,715 bp [1] End 109,573,580 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 F Start 114,569,095 bp [2] End 114,582,121 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver right adrenal cortex left adrenal gland left adrenal cortex apex of heart C1 segment pancreatic ductal cell mucosa of transverse colon right auricle of heart olfactory zone of nasal mucosa Top expressed in lumbar spinal ganglion muscle of thigh interventricular septum otic vesicle neural layer of retina saccule right kidney ascending aorta myocardium of ventricle neural tube More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding cob(I)yrinic acid a,c-diamide adenosyltransferase activity ATP binding protein binding cobalamin binding Cellular component mitochondrial matrix mitochondrion Biological process cobalamin metabolic process cobalamin biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 326625 77697 Ensembl ENSG00000139428 ENSMUSG00000029575 UniProt Q96EY8 Q9D273 RefSeq (mRNA) NM_052845 NM_029956 NM_001347398 RefSeq (protein) NP_443077 NP_001334327 NP_084232 Location (UCSC) Chr 12: 109.55 – 109.57 Mb Chr 5: 114.57 – 114.58 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial is an enzyme that in humans is encoded by the MMAB gene. ^{[5] [6] [7]}

Function

This gene encodes an enzyme (cob(I)yrinic acid a,c-diamide adenosyltransferase) that catalyzes the final step in the conversion of vitamin B₁₂ into adenosylcobalamin (AdoCbl), a vitamin B₁₂-containing coenzyme for methylmalonyl-CoA mutase. ^[7]

Clinical significance

Mutations in the gene are the cause of vitamin B₁₂-dependent methylmalonic aciduria linked to the cblB complementation group. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000139428 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029575 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Dobson CM, Wai T, Leclerc D, Kadir H, Narang M, Lerner-Ellis JP, et al. (December 2002). "Identification of the gene responsible for the cblB complementation group of vitamin B12-dependent methylmalonic aciduria". Human Molecular Genetics. 11 (26): 3361–3369. doi: 10.1093/hmg/11.26.3361 . PMID   12471062.
6. Leal NA, Park SD, Kima PE, Bobik TA (March 2003). "Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant". The Journal of Biological Chemistry. 278 (11): 9227–9234. doi: 10.1074/jbc.M212739200 . PMID   12514191.
7. "Entrez Gene: MMAB methylmalonic aciduria (cobalamin deficiency) cblB type".

External links

• GeneReviews/NCBI/NIH/UW entry on Methylmalonic Acidemia
• PDBe-KB provides an overview of all the structure information available in the PDB for Human Corrinoid adenosyltransferase (MMAB)

Further reading

• Willer CJ, Sanna S, Jackson AU, Scuteri A, Bonnycastle LL, Clarke R, et al. (February 2008). "Newly identified loci that influence lipid concentrations and risk of coronary artery disease". Nature Genetics. 40 (2): 161–169. doi:10.1038/ng.76. PMC   5206900 . PMID   18193043.
• Hörster F, Baumgartner MR, Viardot C, Suormala T, Burgard P, Fowler B, et al. (August 2007). "Long-term outcome in methylmalonic acidurias is influenced by the underlying defect (mut0, mut-, cblA, cblB)". Pediatric Research. 62 (2): 225–230. doi: 10.1203/PDR.0b013e3180a0325f . PMID   17597648.
• Keeratichamroen S, Cairns JR, Sawangareetrakul P, Liammongkolkul S, Champattanachai V, Srisomsap C, et al. (June 2007). "Novel mutations found in two genes of thai patients with isolated methylmalonic acidemia". Biochemical Genetics. 45 (5–6): 421–430. CiteSeerX   10.1.1.509.517 . doi:10.1007/s10528-007-9085-y. PMID   17410422. S2CID   20799098.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, et al. (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC   1356129 . PMID   16344560.
• Martínez MA, Rincón A, Desviat LR, Merinero B, Ugarte M, Pérez B (April 2005). "Genetic analysis of three genes causing isolated methylmalonic acidemia: identification of 21 novel allelic variants". Molecular Genetics and Metabolism. 84 (4): 317–325. doi:10.1016/j.ymgme.2004.11.011. PMID   15781192.
• Leal NA, Olteanu H, Banerjee R, Bobik TA (November 2004). "Human ATP:Cob(I)alamin adenosyltransferase and its interaction with methionine synthase reductase". The Journal of Biological Chemistry. 279 (46): 47536–47542. doi: 10.1074/jbc.M405449200 . PMID   15347655.
• Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC (September 1994). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. hdl: 10669/15162 . PMID   7829101.